Cloning of the mouse gene for d-dopachrome tautomerase

Kuriyama, Taisuke; Fujinaga, Mami; Koda, Toshiaki; Nishihira, Jun

doi:10.1016/s0167-4838(98)00214-3

Cited by 10 publications

(7 citation statements)

References 21 publications

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“…X‐ray crystallography showed MIF to be a trimer of three identical subunits 15 , 16 , 17 and to represent a new structural superfamily. Other members of this superfamily are D‐dopachrome tautomerase (a protein with largely unknown function) 18 and the bacterial enzymes 4‐oxalocrotonate tautomerase (4‐OT) and 5‐carboxymethyl‐2‐hydroxymuconate isomerase (CHMI) 19 …”

Section: Overview Of the Biology Of Mifmentioning

confidence: 99%

Neuroendocrine properties of macrophage migration inhibitory factor (MIF)

Fingerle‐Rowson¹,

Bucala²

2001

Immunol Cell Biol

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SummaryThe cytokine macrophage migration inhibitory factor (MIF) is produced by neuroendocrine and immune tissues and possesses several features that allow it to be characterized as a neuroendocrine mediator. Its pro-inflammatory action and its pathogenic role in inflammatory diseases, such as septic shock, arthritis and other diseases, have clearly been demonstrated and may be based in part on neuroendocrine mechanisms. Macrophage migration inhibitory factor possesses glucocorticoid-antagonist properties within the immune system and participates in the regulation of several endocrine circuits. This review summarizes the current state of MIF research and focuses on MIF expression and function in nervous and endocrine tissues.

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Section: Overview Of the Biology Of Mifmentioning

confidence: 99%

Neuroendocrine properties of macrophage migration inhibitory factor (MIF)

Fingerle‐Rowson¹,

Bucala²

2001

Immunol Cell Biol

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“…The enzyme catalyses two distinct reactions, the conversion of tyrosine to 3,4dihydroxyphenylalanine (Dopa) by tyrosine hydroxylase activity (EC 1.14.18.1) and the oxidation of Dopa to dopaquinone by Dopa oxidase activity (EC 1.10.3.1) (Winder and Harris, 1991). The resultant dopaquinone is nonenzymatically converted to dopachrome, which is further metabolized by an isomerase producing dihydroxyindoles (Kuriyama et al, 1998). Melanin pigments are produced eventually by further oxidation and polymerization of the indoles (Riley, 1997).…”

Section: Introductionmentioning

confidence: 99%

Manassantin A and B fromSaururus chinensisinhibiting cellular melanin production

Seo¹,

Lee²,

Chung³

et al. 2009

Phytotherapy Research

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Hyperpigmentation disorders such as freckles and senile lentigines in the skin are associated with abnormal accumulation of melanin pigments. In this study, two lignan constituents were isolated from Saururus chinensis Baill (Saururaceae) as inhibitors of cellular melanin production by bioassay-guided fractionations. The active constituents were manassantin A and B that dose-dependently inhibited melanin production in alpha-melanocyte stimulating hormone (alpha-MSH)-activated melanoma B16 cells with IC(50) values of 13 nm and 8 nm, respectively. Arbutin as a positive control exhibited an IC(50) value of 96 microm on alpha-MSH-induced melanin production. Further, manassantin A inhibited forskolin- or 3-isobutyl-1-methylxanthine (IBMX)-induced melanin production with IC(50) values of 14 nm or 12 nm, respectively. Manassantin A decreased cellular amounts of IBMX-inducible tyrosinase protein but could not affect the catalytic activity of cell-free tyrosinase, a key enzyme in the biosynthetic pathway of melanin pigments. Finally, this study could provide a pharmacological potential of S. chinensis in hyperpigmentation disorders.

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“…The enzyme oxidizes phenols and diphenols using a catalytic mechanism that depends on the presence of copper atoms at the active site (3,4). Dopaquinone produced by tyrosinase is nonenzymatically converted to dopachrome, which is acted upon by an isomerase producing dihydroxyindoles (5,6). Melanin pigments are eventually produced by further oxidation and polymerization of the indoles (7).…”

mentioning

confidence: 99%

Oxyresveratrol and Hydroxystilbene Compounds

Kim

Yun

Lee

et al. 2002

Journal of Biological Chemistry

282

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Tyrosinase is responsible for the molting process in insects, undesirable browning of fruits and vegetables, and coloring of skin, hair, and eyes in animals. To clarify the mechanism of the depigmenting property of hydroxystilbene compounds, inhibitory actions of oxyresveratrol and its analogs on tyrosinases from mushroom and murine melanoma B-16 have been elucidated in this study. Oxyresveratrol showed potent inhibitory effect with an IC 50 value of 1.2 M on mushroom tyrosinase activity, which was 32-fold stronger inhibition than kojic acid, a depigmenting agent used as the cosmetic material with skin-whitening effect and the medical agent for hyperpigmentation disorders. Hydroxystilbene compounds of resveratrol, 3,5-dihydroxy-4 -methoxystilbene, and rhapontigenin also showed more than 50% inhibition at 100 M on mushroom tyrosinase activity, but other methylated or glycosylated hydroxystilbenes of 3,4 -dimethoxy-5-hydroxystilbene, trimethylresveratrol, piceid, and rhaponticin did not inhibit significantly. None of the hydroxystilbene compounds except oxyresveratrol exhibited more than 50% inhibition at 100 M on L-tyrosine oxidation by murine tyrosinase activity; oxyresveratrol showed an IC 50 value of 52.7 M on the enzyme activity. The kinetics and mechanism for inhibition of mushroom tyrosinase exhibited the reversibility of oxyresveratrol as a noncompetitive inhibitor with L-tyrosine as the substrate. The interaction between oxyresveratrol and tyrosinase exhibited a high affinity reflected in a K i value of 3.2-4.2 ؋ 10 ؊7 M. Oxyresveratrol did not affect the promoter activity of the tyrosinase gene in murine melanoma B-16 at 10 and 100 M. Therefore, the depigmenting effect of oxyresveratrol works through reversible inhibition of tyrosinase activity rather than suppression of the expression and synthesis of the enzyme. The number and position of hydroxy substituents seem to play an important role in the inhibitory effects of hydroxystilbene compounds on tyrosinase activity.Tyrosinase catalyzes two distinct reactions of the conversion of tyrosine to Dopa 1 (tyrosine hydroxylase activity (EC 1.14.18.1); tyrosine, 3,4-dihydroxyphenylalanine, oxygen, and oxidoreductase) and the oxidation of the resultant Dopa (Dopa oxidase activity (EC 1.10.3.1); Dopa, oxygen, and oxidoreductase) (1, 2). The enzyme oxidizes phenols and diphenols using a catalytic mechanism that depends on the presence of copper atoms at the active site (3, 4). Dopaquinone produced by tyrosinase is nonenzymatically converted to dopachrome, which is acted upon by an isomerase producing dihydroxyindoles (5, 6). Melanin pigments are eventually produced by further oxidation and polymerization of the indoles (7).Tyrosinase, an enzyme catalyzing the rate-limiting step for the biosynthetic pathway of melanin pigments, is widely distributed in nature. It exists in many organisms with slightly different forms. The enzyme participates in several important reactions of host defense, wound healing, and sclerotization in insects and other arthropods (8 -10). E...

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Cloning of the mouse gene for d-dopachrome tautomerase

Cited by 10 publications

References 21 publications

Neuroendocrine properties of macrophage migration inhibitory factor (MIF)

Neuroendocrine properties of macrophage migration inhibitory factor (MIF)

Manassantin A and B fromSaururus chinensisinhibiting cellular melanin production

Oxyresveratrol and Hydroxystilbene Compounds

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